Research workbench
Structure of importin a2 bound to p65-NLS
Analyse Structure of importin a2 bound to p65-NLS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LEU
- Type
- protein
- Length
- 437 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.82
- Source
- Mus musculus; SYNTHETIC CONSTRUCT
- Molecule
- Importin subunit alpha-1; Transcription factor p65
- UniProt
- P52293, Q04206
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · resolution 2.82 · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Importin subunit alpha-1 | protein | 423 | 74% helix, 0% strand | P52293 |
| B | Transcription factor p65 | protein | 8 | 0% helix, 0% strand | Q04206 |
| C | Transcription factor p65 | protein | 6 | 0% helix, 0% strand | Q04206 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.48 | 0.83 | 13 | empty |
Interfaces
2 interfaces between chains.
- E–B · 767 Ų buried · 13 hydrogen bonds · protein-protein
- E–C · 630 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7LEU · Structure of importin A2 bound to P65-nls · the same entry in another collection · chain B against B, TM-score 1.00
- P52293 · AlphaFold monomer V2.0 prediction for importin subunit alpha-1 (P52293) · a predicted model of the same protein · chain E against A, TM-score 0.99
- Q04206 · AlphaFold monomer V2.0 prediction for transcription factor P65 (Q04206) · a predicted model of the same protein · chain C against A, TM-score 0.60
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P52293
- Every structure of UniProt Q04206
- Elsewhere: RCSB PDB 7LEU · PDBe 7LEU · UniProt P52293 · UniProt Q04206
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